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> home > Products > Primary Antibodies > Antibody Collections > Zebrafish > (DANRE) hspa8 Antibody (C-term)
(DANRE) hspa8 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, E |
|---|---|
| Primary Accession | Q90473 |
| Reactivity | Human, Mouse, Zebrafish |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Clone/Animal Names | RB49652 |
| Calculated MW | 70974 Da |
| Other Names | Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8, hspa8, hsc70 |
|---|---|
| Target/Specificity | This DANRE hspa8 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 458-490 amino acids from the C-terminal region of DANRE hspa8. |
| Dilution | WB~~1:2000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | (DANRE) hspa8 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | hspa8 {ECO:0000250|UniProtKB:P11142} |
|---|---|
| Function | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Substrate recognition component in chaperone- mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (By similarity). May play a role in uncoating of clathrin- coated vesicles (By similarity). |
| Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P11142} |
Research Areas
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Application Protocols
Provided below are standard protocols that you may find useful for product applications.
References
Graser R.T.,et al.Genetica 98:273-276(1996).
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$ 140.00
Cat# Azb21567b
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